ID   MTMW_METWO              Reviewed;         668 AA.
AC   O59647;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Type II methyltransferase M.MwoI {ECO:0000303|PubMed:12654995};
DE            Short=M.MwoI {ECO:0000303|PubMed:2663652};
DE            EC=2.1.1.113;
DE   AltName: Full=Modification methylase MwoI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase MwoI;
GN   Name=mwoIM {ECO:0000303|PubMed:2663652};
OS   Methanothermobacter wolfeii (Methanobacterium wolfei).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=145261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43096 / DSM 2970 / JCM 14652 / NBRC 100332 / VKM B-1829;
RA   Lunnen K.D., Wilson G.G.;
RT   "Method for producing the MwoI restriction endonuclease and methylase.";
RL   Patent number US5053330, 01-OCT-1991.
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 43096 / DSM 2970 / JCM 14652 / NBRC 100332 / VKM B-1829;
RX   PubMed=2663652; DOI=10.1016/0378-1119(89)90354-5;
RA   Lunnen K.D., Morgan R.D., Timan C.J., Krzycki J.A., Reeve J.N.,
RA   Wilson G.G.;
RT   "Characterization and cloning of MwoI (GCN7GC), a new type-II restriction-
RT   modification system from Methanobacterium wolfei.";
RL   Gene 77:11-19(1989).
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A beta subtype methylase, recognizes the double-stranded DNA
CC       sequence 5'-GCNNNNNNNGC-3', methylates C-2 on both strands, and
CC       protects the DNA from cleavage by the MwoI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2663652}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF051376; AAC05700.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59647; -.
DR   SMR; O59647; -.
DR   REBASE; 3451; M.MwoI.
DR   PRIDE; O59647; -.
DR   BRENDA; 2.1.1.113; 3258.
DR   PRO; PR:O59647; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..668
FT                   /note="Type II methyltransferase M.MwoI"
FT                   /id="PRO_0000087930"
SQ   SEQUENCE   668 AA;  77723 MW;  7F5B53A2807912D3 CRC64;
     MVKGKILFGD VFSALRCLED NSISVALTSP PYWRQRDYGF KGQIGREKTP EEYIGRLIVI
     FRELRAKLKD DGVFFLNIGD KYKNRYGKSH LLQIPYRLAA HMIKDGWKLL DIIIWYKPNH
     MPSSVKDRFT NTYEPVLVFG KSDENIYTKK HPVLKIPLQQ TKWKHTAVFP EKLVSSLLSR
     CNLKDGDYIL DPFAGTGTTG AVVKKMKYQL YPKDLNVILI EKGKKFLDII TERTGIKEIK
     ELKSSEYTWE PVNDKLAFSE DKPLIIIEDT HGETFIAKNS EEFSRIIMGM LSEEFQDFHR
     EDAVYFFGVK NWKLSDLVLP GLLIDHGFIL RNMIIIEDGS SWYPVFMLVK DTTRVNYKFY
     IDRIRKKPKT VLPEKWNQED FIGLIVNDNL SKKPRKGEVV DIISTYSQDN FPKIVAVSWE
     DDNISLELCL NPRKDEFIME SLQFTCPHCG TQLIDTYDPL GDNICYNCQK EIYGKNSLPI
     LKESKEIIES LESVENGEYQ VGENIKPQYQ KRCKESKSKF AGMERMNWGA SPGARKTIIG
     DSFSKMRLYR LDQPTIARYL NIYMKKNDLR IKDITQALPP EYKHTVGHWF RKDFGGSIPL
     PEDVTLLEEI LKLDKEFARI LKRSVLKLQT VKHSLKGKNP GDFLELEENK LKEYLTKTYM
     PPSYYIKK